4hqk

Crystal structure of Plasmodium falciparum TRAP, P4212 form

spinqualitylabelsall models 4hqk, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4hqk is a 2 chain structure with sequence from Plasmodium falciparum 3D7. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.249Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q76NM2_PLAF7 Publication Abstract from PubMed Sporozoite gliding motility and invasion of mosquito and vertebrate host cells in malaria is mediated by thrombospondin repeat anonymous protein (TRAP). Tandem von Willebrand factor A (VWA) and thrombospondin type I repeat (TSR) domains in TRAP connect through proline-rich stalk, transmembrane, and cytoplasmic domains to the parasite actin-dependent motility apparatus. We crystallized fragments containing the VWA and TSR domains from Plasmodium vivax and Plasmodium falciparum in different crystal lattices. TRAP VWA domains adopt closed and open conformations, and bind a Mg(2+) ion at a metal ion-dependent adhesion site implicated in ligand binding. Metal ion coordination in the open state is identical to that seen in the open high-affinity state of integrin I domains. The closed VWA conformation associates with a disordered TSR domain. In contrast, the open VWA conformation crystallizes with an extensible beta ribbon and ordered TSR domain. The extensible beta ribbon is composed of disulfide-bonded segments N- and C-terminal to the VWA domain that are largely drawn out of the closed VWA domain in a 15 A movement to the open conformation. The extensible beta ribbon and TSR domain overlap at a conserved interface. The VWA, extensible beta ribbon, and TSR domains adopt a highly elongated overall orientation that would be stabilized by tensile force exerted across a ligand-receptor complex by the actin motility apparatus of the sporozoite. Our results provide insights into regulation of "stick-and-slip" parasite motility and for development of sporozoite subunit vaccines. Shape change in the receptor for gliding motility in Plasmodium sporozoites.,Song G, Koksal AC, Lu C, Springer TA Proc Natl Acad Sci U S A. 2012 Dec 26;109(52):21420-5. doi:, 10.1073/pnas.1218581109. Epub 2012 Dec 11. PMID:23236185 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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